Improvement of the Off-flavor of Soy Protein Isolate by Removing Oil-body Associated Proteins and Polar Lipids

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概要

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• The precipitate formed by ultracentrifuging a defatted soybean extract at 200,000×g for 50 min at pH 7.5 was composed of particles of 100-200 nm in diameter and enriched with 34-kDa, 24-kDa and 18-kDa proteins. An SDS-PAGE analysis showed these proteins to migrate to a position identical to that of oil-body-associated proteins (OBAPs ; Herman, Planta, 172,336-345,1987).^<1)> They were recovered in the precipitate of soy protein with 30-40% saturated ammonium sulfate in the presence of 10 mM 2-ME. The lipid composition of the precipitate by a TLC analysis showed that most of the polar lipids in the soybean extract had been condensed in the fraction, suggesting the association between OBAP and the polar lipids. Removal of OBAP and the polar lipids from the soybean extract by conventional centrifugation (10,000×g for 10 min) in the presence of 30 mM Na_2SO_4 and 30 mM CaCl_2 at pH 2.8 was achieved with concomitant improvement of the volatile off-flavor. A soy protein isolate (SPI) prepared from such a soybean extract contained far fewer volatile off-flavor compounds than normal SPI did.

• 社団法人日本農芸化学会の論文
• 1998-05-23

著者

• Kawamura Yukio

  Protein Science Laboratory National Food Research Institute

• SAMOTO Masahiko

  Central Research Institute, Fuji Oil Co.

• Miyazaki Chiaki

  Fuji Co. Ltd

• Miyazaki Chiaki

  Central Research Institute Fuji Oil Co. Ltd.

• Akasaka Takeshi

  Central Research Institute Fuji Oil Co., Ltd.

• Samoto Masahiko

  Protein Development R&d Division Fuji Oil Co. Ltd.

• KANAMORI Jiroh

  Central Research Institute, Fuji Oil Co. Ltd.

• Akasaka Takeshi

  Central Research Institute Fuji Oil Co. Ltd.

• Kanamori Jiroh

  Central Research Institute Fuji Oil Co. Ltd.

関連論文

• Substantially Complete Removal of Three Major Allergenic Soybean Proteins (Gly m Bd 30K, Gly m Bd 28K, and the α-Subunit of Conglycinin) from Soy Protein by Using a Mutant Soybean, Tohoku 124
• Protein Disulfide Isomerase Activity of Some Plant Seeds
• Substantially Complete Removal of the 34 kDa Allergenic Soybean Protein, Gly m Bd 30 K, from Soy Milk of a Mutant Lacking the α- and α'-Subunits of Conglycinin
• Purification and Characterizationof Protein Disulfide Isomerase from Soybeam
• Simple and Efficient Procedure for Removing the 34kDa Allergenic Soybean Protein, Gly m I, from Defatted Soy Milk
• Soybean Allergens and Hypoallergenic Soybean Products
• Improvement of the Off-flavor of Soy Protein Isolate by Removing Oil-body Associated Proteins and Polar Lipids
• Specific Binding of Allergenic Soybean Protein Gly m Bd 30K with α'- and α-Subunits of Conglycinin in Soy Milk
• Effects of Soybean β-Conglycinin on Body Fat Ratio and Serum Lipid Levels in Healthy Volunteers of Female University Students
• Effects of Soybean β-Conglycinin (7S Globulin) on Postprandial Serum Lipids (Lipid Disorders 5 (H), The 69th Annual Scientific Meeting of the Japanese Circulation Society)
• Phosphoenolpyruvate Carboxylase Level in Soybean Seed Highly Correlates to Its Contents of Protein and Lipid(Biological Chemistry)

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